Synthesis and Characterization of Potent Bivalent Amyloidosis Inhibitors That Bind Prior to Transthyretin Tetramerization-Reference-Cited by-同舟云学术

Synthesis and Characterization of Potent Bivalent Amyloidosis Inhibitors That Bind Prior to Transthyretin Tetramerization

Published:2003-10-01 Issue:44 Volume:125 Page:13404-13414
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Green Nora S.¹,Palaninathan Satheesh K.¹,Sacchettini James C.¹,Kelly Jeffery W.¹

Affiliation:

1. Contribution from the Department of Chemistry and Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, BCC265, La Jolla, California 92037, and Department of Biochemistry and Biophysics, Texas A&M University, College Station, Texas 77843-2128

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja030294z

Reference44 articles.

1. An X-ray study of the subunit structure of prealbumin

2. Structure of prealbumin: Secondary, tertiary and quaternary interactions determined by Fourier refinement at 1.8 Å

3. Structure of a complex of two plasma proteins: transthyretin and retinol-binding protein

4. Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitro

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